P21243 (PSA6_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Proteasome component C7-alpha
EC=3.4.25.1

Alternative name(s):
Macropain subunit C7-alpha
Multicatalytic endopeptidase complex C7
Proteasome component Y8
Proteinase YSCE subunit 7
SCL1 suppressor protein

Gene names

Name:	SCL1
Synonyms:	PRC2, PRS2
Ordered Locus Names:	YGL011C

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length	252 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	The proteasome degrades poly-ubiquitinated proteins in the cytoplasm and in the nucleus. It is essential for the regulated turnover of proteins and for the removal of misfolded proteins. The proteasome is a multicatalytic proteinase complex that is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. It has an ATP-dependent proteolytic activity.
Catalytic activity	Cleavage of peptide bonds with very broad specificity.
Subunit structure	The 26S proteasome consists of a 20S proteasome core and two 19S regulatory subunits. The 20S proteasome core is composed of 28 subunits that are arranged in four stacked rings, resulting in a barrel-shaped structure. The two end rings are each formed by seven alpha subunits, and the two central rings are each formed by seven beta subunits. The catalytic chamber with the active sites is on the inside of the barrel. Interacts with CIC1. Ref.7
Subcellular location	Cytoplasm. Nucleus Ref.8.
Miscellaneous	Present with 15200 molecules/cell in log phase SD medium. Ref.9
Sequence similarities	Belongs to the peptidase T1A family.
Sequence caution	The sequence AAA35020.1 differs from that shown. Reason: Frameshift at position 26.

Ontologies

Keywords
Cellular component	Cytoplasm Nucleus Proteasome
Molecular function	Hydrolase Protease Threonine protease
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	proteasomal ubiquitin-dependent protein catabolic process Inferred from direct assay. Source: SGD proteasomal ubiquitin-independent protein catabolic process Inferred from direct assay. Source: SGD
Cellular component	mitochondrion Inferred from direct assay. Source: SGD nuclear outer membrane-endoplasmic reticulum membrane network Inferred by curator Ref.11. Source: SGD nucleus Inferred by curator Ref.11. Source: SGD proteasome core complex, alpha-subunit complex Inferred from direct assay Ref.11. Source: SGD proteasome storage granule Inferred by curator Ref.11. Source: SGD
Molecular function	protein binding Inferred from physical interaction. Source: IntAct threonine-type endopeptidase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
PRE10	P21242	5	EBI-13975,EBI-13963
PRE8	P23639	5	EBI-13975,EBI-13959

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 252

252

Proteasome component C7-alpha

PRO_0000124141

Amino acid modifications

Modified residue

237

1

Phosphoserine Ref.10

Secondary structure

1

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252

Helix Strand Turn

Details...

Helix

11 – 14

4

Beta strand

16 – 18

3

Helix

26 – 34

9

Turn

35 – 38

4

Beta strand

42 – 46

5

Beta strand

48 – 56

9

Helix

66 – 68

3

Beta strand

71 – 74

4

Beta strand

76 – 78

3

Beta strand

80 – 85

6

Helix

87 – 108

22

Helix

114 – 130

17

Beta strand

140 – 147

8

Turn

148 – 150

3

Beta strand

151 – 157

7

Beta strand

163 – 172

10

Helix

175 – 189

15

Beta strand

191 – 193

3

Helix

199 – 214

16

Beta strand

222 – 229

8

Beta strand

232 – 235

4

Helix

238 – 248

11

Sequences

	Sequence		Length	Mass (Da)
	P21243 [UniParc]. Last modified May 1, 1991. Version 1. Checksum: 5B938C862BC8D7EB	FASTA	252	28,001
	10 20 30 40 50 60 MSGAAAASAA GYDRHITIFS PEGRLYQVEY AFKATNQTNI NSLAVRGKDC TVVISQKKVP 70 80 90 100 110 120 DKLLDPTTVS YIFCISRTIG MVVNGPIPDA RNAALRAKAE AAEFRYKYGY DMPCDVLAKR 130 140 150 160 170 180 MANLSQIYTQ RAYMRPLGVI LTFVSVDEEL GPSIYKTDPA GYYVGYKATA TGPKQQEITT 190 200 210 220 230 240 NLENHFKKSK IDHINEESWE KVVEFAITHM IDALGTEFSK NDLEVGVATK DKFFTLSAEN 250 IEERLVAIAE QD

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The suppressor gene scl1+ of Saccharomyces cerevisiae is essential for growth." Balzi E., Chen W., Capieaux E., McCusker J.H., Haber J.E., Goffeau A. Gene 83:271-279(1989) [PubMed: 2684789] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Proteasomes are essential for yeast proliferation. cDNA cloning and gene disruption of two major subunits." Fujiwara T., Tanaka K., Orino E., Yoshimura T., Kumatori A., Tamura T., Chung C.H., Nakai T., Yamaguchi K., Shin S., Kakizuka A., Nakanishi S., Ichihara A. J. Biol. Chem. 265:16604-16613(1990) [PubMed: 1697860] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 174-187 AND 189-198.
[3]	"Molecular cloning and functional analysis of three subunits of yeast proteasome." Emori Y., Tsukahara T., Kawasaki H., Ishiura S., Sugita H., Suzuki K. Mol. Cell. Biol. 11:344-353(1991) [PubMed: 1898763] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE. Strain: ATCC 26786 / X2180-1A.
[4]	"The DNA sequencing of the 17 kb HindIII fragment spanning the LEU1 and ATE1 loci on chromosome VII from Saccharomyces cerevisiae reveals the PDR6 gene, a new member of the genetic network controlling pleiotropic drug resistance." Chen W., Balzi E., Capieaux E., Choder M., Goffeau A. Yeast 7:287-299(1991) [PubMed: 1882553] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 46191 / IL125-2B.
[5]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome VII." Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J., Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M., Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L., Coblenz A., Coglievina M., Coissac E. , Defoor E., Del Bino S., Delius H., Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P., Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M., Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A., Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K., Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P., Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E., Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K., Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A., Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S., Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M., Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C., Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M., Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M., Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y., Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L., Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D., Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F., Zaccaria P., Zimmermann M., Zollner A., Kleine K. Nature 387:81-84(1997) [PubMed: 9169869] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 96604 / S288c / FY1679.
[6]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[7]	"Cic1, an adaptor protein specifically linking the 26S proteasome to its substrate, the SCF component Cdc4." Jaeger S., Strayle J., Heinemeyer W., Wolf D.H. EMBO J. 20:4423-4431(2001) [PubMed: 11500370] [Abstract] Cited for: INTERACTION WITH CIC1.
[8]	"Global analysis of protein localization in budding yeast." Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K. Nature 425:686-691(2003) [PubMed: 14562095] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[9]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed: 14562106] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[10]	"A multidimensional chromatography technology for in-depth phosphoproteome analysis." Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H. Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed: 18407956] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-237, MASS SPECTROMETRY.
[11]	"Structure of 20S proteasome from yeast at 2.4-A resolution." Groll M., Ditzel L., Loewe J., Stock D., Bochtler M., Bartunik H.D., Huber R. Nature 386:463-471(1997) [PubMed: 9087403] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 10-252 OF COMPLEX WITH THE 20S PROTEASOME.
[12]	"Structural basis for the activation of 20S proteasomes by 11S regulators." Whitby F.G., Masters E.I., Kramer L., Knowlton J.R., Yao Y., Wang C.C., Hill C.P. Nature 408:115-120(2000) [PubMed: 11081519] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF COMPLEX WITH THE 20S PROTEASOME.
[13]	"A gated channel into the proteasome core particle." Groll M., Bajorek M., Koehler A., Moroder L., Rubin D.M., Huber R., Glickman M.H., Finley D. Nat. Struct. Biol. 7:1062-1067(2000) [PubMed: 11062564] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 10-252 OF COMPLEX WITH THE 20S PROTEASOME.
[14]	"Crystal structure of the 20 S proteasome:TMC-95A complex: a non-covalent proteasome inhibitor." Groll M., Koguchi Y., Huber R., Kohno J. J. Mol. Biol. 311:543-548(2001) [PubMed: 11493007] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 10-252 OF COMPLEX WITH THE 20S PROTEASOME.
[15]	"TMC-95-based inhibitor design provides evidence for the catalytic versatility of the proteasome." Groll M., Goetz M., Kaiser M., Weyher E., Moroder L. Chem. Biol. 13:607-614(2006) [PubMed: 16793518] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.81 ANGSTROMS) OF 10-252 OF COMPLEX WITH THE 20S PROTEASOME.
[16]	"Crystal structures of salinosporamide A (NPI-0052) and B (NPI-0047) in complex with the 20S proteasome reveal important consequences of beta-lactone ring opening and a mechanism for irreversible binding." Groll M., Huber R., Potts B.C.M. J. Am. Chem. Soc. 128:5136-5141(2006) [PubMed: 16608349] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 10-252 OF COMPLEX WITH THE 20S PROTEASOME.
[17]	"Crystal structure of the boronic acid-based proteasome inhibitor bortezomib in complex with the yeast 20S proteasome." Groll M., Berkers C.R., Ploegh H.L., Ovaa H. Structure 14:451-456(2006) [PubMed: 16531229] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 10-252 OF COMPLEX WITH THE 20S PROTEASOME.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M31430 Genomic DNA. Translation: AAA35020.1. Frameshift.
X56971 Genomic DNA. Translation: CAA40292.1.
M55440 mRNA. Translation: AAA35228.1.
M63641 Genomic DNA. Translation: AAA34909.1.
X56732 Genomic DNA. Translation: CAA40056.1.
S58126 Genomic DNA. Translation: AAD13894.1.
Z72533 Genomic DNA. Translation: CAA96711.1.
BK006941 Genomic DNA. Translation: DAA08087.1.

PIR

SNBYS1. S11199.

RefSeq

NP_011504.1. NM_001180876.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1FNT	X-ray	3.20	A/O	1-252	[»]
1G0U	X-ray	2.40	G/U	1-252	[»]
1G65	X-ray	2.25	G/U	10-252	[»]
1JD2	X-ray	3.00	2/G	10-252	[»]
1RYP	X-ray	1.90	A/O	10-252	[»]
1VSY	X-ray	3.00	A/O	10-252	[»]
1Z7Q	X-ray	3.22	A/O	1-252	[»]
2F16	X-ray	2.80	G/U	10-252	[»]
2FAK	X-ray	2.80	G/U	10-252	[»]
2GPL	X-ray	2.81	G/U	10-252	[»]
2ZCY	X-ray	2.90	G/U	1-252	[»]
3BDM	X-ray	2.70	G/U	1-252	[»]
3D29	X-ray	2.60	G/U	12-252	[»]
3DY3	X-ray	2.81	G/U	10-252	[»]
3DY4	X-ray	2.80	G/U	10-252	[»]
3E47	X-ray	3.00	G/U	10-252	[»]
3GPJ	X-ray	2.70	G/U	10-252	[»]
3GPT	X-ray	2.41	G/U	10-252	[»]
3GPW	X-ray	2.50	G/U	10-252	[»]
3HYE	X-ray	2.50	G/U	10-252	[»]
3L5Q	X-ray	3.00	A/C	10-252	[»]
3MG0	X-ray	2.68	G/U	10-252	[»]
3MG4	X-ray	3.11	G/U	10-252	[»]
3MG6	X-ray	2.60	G/U	1-252	[»]
3MG7	X-ray	2.78	G/U	1-252	[»]
3MG8	X-ray	2.59	G/U	1-252	[»]
3NZJ	X-ray	2.40	G/U	1-252	[»]
3NZW	X-ray	2.50	G/U	1-252	[»]
3NZX	X-ray	2.70	G/U	1-252	[»]
3OEU	X-ray	2.60	G/U	10-252	[»]
3OEV	X-ray	2.85	G/U	10-252	[»]
3OKJ	X-ray	2.70	G/U	10-252	[»]
3TDD	X-ray	2.70	G/U	10-252	[»]

ProteinModelPortal

P21243.

SMR

P21243. Positions 10-252.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-2810N.

IntAct

P21243. 32 interactions.

MINT

MINT-525412.

STRING

P21243.

Protein family/group databases

MEROPS

T01.971.

2D gel databases

UCD-2DPAGE

P21243.

Proteomic databases

PeptideAtlas

P21243.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblFungi

YGL011C; YGL011C; YGL011C.

GeneID

852873.

KEGG

sce:YGL011C.

NMPDR

fig|4932.3.peg.2612.

Organism-specific databases

CYGD

YGL011c.

SGD

S000002979. SCL1.

Phylogenomic databases

eggNOG

fuNOG07535.

GeneTree

EFGT00050000002415.

HOGENOM

HBG499923.

OMA

GKDCAVV.

OrthoDB

EOG4FXVHG.

Gene expression databases

ArrayExpress

P21243.

Genevestigator

P21243.

GermOnline

YGL011C. Saccharomyces cerevisiae.

Family and domain databases

InterPro

IPR000426. Proteasome_asu_N.
IPR023332. Proteasome_suA-type.
IPR001353. Proteasome_sua/b.
[Graphical view]

KO

K02730.

Pfam

PF00227. Proteasome. 1 hit.
PF10584. Proteasome_A_N. 1 hit.
[Graphical view]

SMART

SM00948. Proteasome_A_N. 1 hit.
[Graphical view]

PROSITE

PS00388. PROTEASOME_A_1. 1 hit.
PS51475. PROTEASOME_A_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

NextBio

972505.

Entry information

Entry name

PSA6_YEAST

Accession

Primary (citable) accession number: P21243
Secondary accession number(s): D6VUC6, P15708

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 1, 1991
Last sequence update:	May 1, 1991
Last modified:	January 25, 2012
This is version 139 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program